CAD1 and CCR2 protein complex formation in monolignol biosynthesis in Populus trichocarpa

CAD1 and CCR2 protein complex formation in monolignol biosynthesis in Populus trichocarpa

© 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 222(2019), 1 vom: 01. Apr., Seite 244-260
1. Verfasser: Yan, Xiaojing (VerfasserIn)
Weitere Verfasser: Liu, Jie, Kim, Hoon, Liu, Baoguang, Huang, Xiong, Yang, Zhichang, Lin, Ying-Chung Jimmy, Chen, Hao, Yang, Chenmin, Wang, Jack P, Muddiman, David C, Ralph, John, Sederoff, Ronald R, Li, Quanzi, Chiang, Vincent L
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Populus trichocarpa co-immunoprecipitation enzyme activity monolignol biosynthetic pathway nuclear magnetic resonance (NMR) stem-differentiating xylem protein Plant Proteins mehr... Recombinant Proteins Lignin 9005-53-2 Aldehyde Oxidoreductases EC 1.2.- cinnamoyl CoA reductase EC 1.2.1.44
Beschreibung
Zusammenfassung:© 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.
Lignin is the major phenolic polymer in plant secondary cell walls and is polymerized from monomeric subunits, the monolignols. Eleven enzyme families are implicated in monolignol biosynthesis. Here, we studied the functions of members of the cinnamyl alcohol dehydrogenase (CAD) and cinnamoyl-CoA reductase (CCR) families in wood formation in Populus trichocarpa, including the regulatory effects of their transcripts and protein activities on monolignol biosynthesis. Enzyme activity assays from stem-differentiating xylem (SDX) proteins showed that RNAi suppression of PtrCAD1 in P. trichocarpa transgenics caused a reduction in SDX CCR activity. RNAi suppression of PtrCCR2, the only CCR member highly expressed in SDX, caused a reciprocal reduction in SDX protein CAD activities. The enzyme assays of mixed and coexpressed recombinant proteins supported physical interactions between PtrCAD1 and PtrCCR2. Biomolecular fluorescence complementation and pull-down/co-immunoprecipitation experiments supported a hypothesis of PtrCAD1/PtrCCR2 heterodimer formation. These results provide evidence for the formation of PtrCAD1/PtrCCR2 protein complexes in monolignol biosynthesis in planta
Beschreibung:Date Completed 27.02.2020
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.15505